immunofluorescence: 1:10-1:50 western blot: 1:1000
N° accesso UniProt
Condizioni di spedizione
wet ice
Temperatura di conservazione
−20°C
modifica post-traduzionali bersaglio
unmodified
Descrizione generale
Influenza virus hemagglutinin (HA) precursor is encoded by the gene mapped on segment 4. The encoded protein is a 76kDa surface glycoprotein and it exists as trimers on the envelope.
Applicazioni
ANTI-HA TAG antibody produced in rabbit has been used in immunohistochemistry.
Azioni biochim/fisiol
Influenza virus hemagglutinin (HA) acts as a key immunogen in avian influenza virus (AIV) vaccines. Activated HA facilitates virus attachment to oligosaccharide receptors on host cell surface and is involved in penetration through fusion following conformational modifications in the endolysosomal compartment. 226 and 228 residues in HA of the H3 subtype play a key role in host range restriction and receptor specificity.
Stato fisico
Supplied in PBS with 0.09% (W/V) sodium azide
Esclusione di responsabilità
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
Exoenzyme Y (ExoY) is a type III secretion system effector found in 90% of the Pseudomonas aeruginosa isolates. Although it is known that ExoY is a soluble nucleotidyl cyclase that increases the cytoplasmic levels of nucleoside 3',5'-cyclic monophosphates (cNMPs) to
The role of influenza A virus hemagglutinin residues 226 and 228 in receptor specificity and host range restriction.
The catalytic domain of most 'cut and paste' DNA transposases have the canonical RNase-H fold, which is also shared by other polynucleotidyl transferases such as the retroviral integrases and the RAG1 subunit of V(D)J recombinase. The RNase-H fold is a
A single amino acid substitution in 1918 influenza virus hemagglutinin changes receptor binding specificity.
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